Taxonomic group: fungi / Basidiomycota
(Phylum: Basidiomycota)
Organ / tissue: fruiting body
The structure was elucidated in this paperNCBI PubMed ID: 22102286Publication DOI: 10.1074/jbc.M111.297887Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: Xu X <xuxj626

263.net>; Ashida H <ashida

kobe-u.ac.jp>
Institutions: Department of Chemistry, Wuhan University, Wuhan, China, Organization of Advanced Science and Technology, Kobe University, Kobe, Japan, Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Kobe, Japan
Lentinan (LNT), a β-glucan from the fruiting body of Lentinus edodes, is well known to have immunomodulatory activity. NO and TNF-α are associated with many inflammatory diseases. In this study, we investigated the effects of LNT extracted by sonication (LNT-S) on the NO and TNF-α production in LPS-stimulated murine RAW 264.7 macrophages. The results suggested that treatment with LNT-S not only resulted in the striking inhibition of TNF-α and NO production in LPS-activated macrophage RAW 264.7 cells, but also the protein expression of inducible NOS (iNOS) and the gene expression of iNOS mRNA and TNF-α mRNA. It is surprising that LNT-S enhanced LPS-induced NF-κB p65 nuclear translocation and NF-κB luciferase activity, but severely inhibited the phosphorylation of JNK1/2 and ERK1/2. The neutralizing antibodies of anti-Dectin-1 and anti-TLR2 hardly affected the inhibition of NO production. All of these results suggested that the suppression of LPS-induced NO and TNF-α production was at least partially attributable to the inhibition of JNK1/2 and ERK1/2 activation. This work discovered a promising molecule to control the diseases associated with overproduction of NO and TNF-α.
β-glucan, nitric oxide, NF-κB, ERK, Jun N-terminal kinase (JNK), tumor Necrosis Factor (TNF)
Structure type: structural motif or average structure
Location inside paper: p. 871, column 2, paragraph 2
Trivial name: lentinan
Compound class: glucan
Contained glycoepitopes: IEDB_141806,IEDB_142488,IEDB_146664,IEDB_241101,IEDB_983931,SB_192
Methods: ELISA, extraction, cytokine assay, SPR, determination of NO production, centrifugation, filtration, ultrasonication, ANOVA, WEstern blotting, luciferase assay
Biological activity: stimulates natural killer cell activity, macrophage/monocyte functions, phagocytosis, cytotoxicity; suppresses NO and TNF-α production as well as its mRNA in RAW 264.7 cell culture; inhibits iNOS protein expression as well as its mRNA in in RAW 264.7 cell culture; inhibits LPS-induced phosphoryllation of ERK1/2 and JNK1/2; enhances nuclear translocation and transactivation of NF-κB p65
Related record ID(s): 41222, 42037, 42356, 42404, 42451, 42472, 42492, 43481
NCBI Taxonomy refs (TaxIDs): 5353
Show glycosyltransferases
There is only one chemically distinct structure:
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: cell wall
The structure was elucidated in this paperNCBI PubMed ID: 22750202Publication DOI: 10.1016/j.bbagen.2012.06.015Journal NLM ID: 0217513Publisher: Elsevier
Correspondence: Ashida H <ashida

kobe-u.ac.jp>, Xu X <xuxj626

263.net>
Institutions: Department of Chemistry, Wuhan University, Wuhan, China, Organization of Advanced Science and Technology, Kobe University, Kobe, Japan, Department of Agrobioscience, Applied Chemistry in Bioscience Division, Graduate School of Agricultural Science, Kobe University, Kobe, Japan
β-Glucans obtained from fungi, such as baker's yeast (Saccharomyces cerevisiae)-derived β-glucan (BBG), potently activate macrophages through nuclear factor κB (NFκB) translocation and activation of its signaling pathways. The mechanisms by which β-glucans activate these signaling pathways differ from that of lipopolysaccharide (LPS). However, the effects of β-glucans on LPS-induced inflammatory responses are poorly understood. Here, we examined the effects of BBG on LPS-induced inflammatory responses in RAW264.7 mouse macrophages. We explored the actions of BBG in RAW264.7 macrophages. BBG inhibited LPS-stimulated nitric oxide (NO) production in RAW264.7 macrophages by 35-70% at concentrations of 120-200μg/ml. BBG also suppressed mRNA and protein expression of LPS-induced inducible NO synthase (iNOS) and mitogen-activated protein kinase phosphorylation, but not NFκB activation. By contrast, a neutralizing antibody against dectin-1, a β-glucan receptor, did not affect BBG-mediated inhibition of NO production. Meanwhile, BBG suppressed Pam3CSK-induced NO production. Moreover, BBG suppressed LPS-induced production of pro-and anti-inflammatory cytokines, including interleukin (IL)-1α, IL-1ra, and IL-27. Our results indicate that BBG is a powerful inhibitor of LPS-induced NO production by downregulating iNOS expression. The mechanism involves inactivation of mitogen-activated protein kinase and TLR2 pathway, but is independent of dectin-1. BBG might be useful as a novel agent for the chemoprevention of inflammatory diseases.
Lipopolysaccharide, beta-glucan, anti-inflammation, RAW264.7 macrophage, inducible nitric oxide synthase
Structure type: structural motif or average structure
Location inside paper: p. 1657, column 1, paragraph 2
Trivial name: β-1,3-glucan
Compound class: cell wall polysaccharide, glucan
Contained glycoepitopes: IEDB_1397514,IEDB_141806,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_241101,IEDB_558867,IEDB_558868,IEDB_558869,IEDB_857743,IEDB_983931,SB_192
Methods: PCR, Western blotting, cytokine assay, immunological assays, determination of NO production, luciferase assay
Biological activity: recognized by Dectin-1 and toll-like receptors(TLR)-2, that activates immune system; Inhibits NO generation in RAW 264.7 macrophages, enhances NF-κB translocation, attenuates LPS-induced cytokine production
NCBI Taxonomy refs (TaxIDs): 4932Reference(s) to other database(s): GTC:G84939PP
Show glycosyltransferases
There is only one chemically distinct structure: